SH3 domains: modules of protein-protein interactions

Natalya Kurochkina; Udayan Guha

doi:10.1007/s12551-012-0081-z

SH3 domains: modules of protein-protein interactions

Biophys Rev. 2013 Mar;5(1):29-39. doi: 10.1007/s12551-012-0081-z. Epub 2012 Jun 20.

Authors

Natalya Kurochkina¹, Udayan Guha²

Affiliations

¹ Department of Biophysics, The School of Theoretical Modeling, PO Box 15676, Chevy Chase, MD, 20825, USA. info@schtm.org.
² Medical Oncology Branch, National Cancer Institute, National Institutes of Health, Bldg 10, Rm 13 N240-C 10, Center Drive, Bethesda, MD, 20892, USA.

Abstract

Src homology 3 (SH3) domains are involved in the regulation of important cellular pathways, such as cell proliferation, migration and cytoskeletal modifications. Recognition of polyproline and a number of noncanonical sequences by SH3 domains has been extensively studied by crystallography, nuclear magnetic resonance and other methods. High-affinity peptides that bind SH3 domains are used in drug development as candidates for anticancer treatment. This review summarizes the latest achievements in deciphering structural determinants of SH3 function.

Keywords: Cell signaling; Myosin; Protein conformation; SH3 domain; Src-family; Three-dimensional structure.

Publication types

Review